It has long been established that development of conformational structure is dependent on the amino acid sequence, although the exact relationship (which would make possible the precise prediction of native conformation from primary structure, as well as the mechanism by which it forms) still eludes us. It has long been believed that native conformation develops directly from the randomly coiled chain of the denatured protein. Recent observations in several laboratories indicate, however, that denatured chicken egg white lysozyme possesses secondary structure which resembles that of the native protein, although much of the native structure has been destroyed. The present project is an attempt to characterize the structure of reduced lysozyme by its circular dichroic behavior. It has been found that two to three times more beta-structure exists in the reduced chain than is present in the native protein, although alpha-helix is much diminished. The significance of this observation lies largely in the possibility that the reduced structure may function as a "precursor conformation" that would influence the resumption of native structure when the reductive process is reversed (or after synthesis of the reduced chain in the living cell). This investigation will be extended to other proteins.